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Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper.

Publication ,  Journal Article
Thress, K; Song, J; Morimoto, RI; Kornbluth, S
Published in: The EMBO journal
March 2001

Protein folding mediated by the Hsp70 family of molecular chaperones requires both ATP and the co-chaperone Hdj-1. BAG-1 was recently identified as a bcl-2-interacting, anti-apoptotic protein that binds to the ATPase domain of Hsp70 and prevents the release of the substrate. While this suggested that cells had the potential to modulate Hsp70-mediated protein folding, physiological regulators of BAG-1 have yet to be identified. We report here that the apoptotic regulator Scythe, originally isolated through binding to the potent apoptotic inducer Reaper, shares limited sequence identity with BAG-1 and inhibits Hsp70- mediated protein refolding. Scythe-mediated inhibition of Hsp70 is reversed by Reaper, providing evidence for the regulated reversible inhibition of chaperone activity. As Scythe functions downstream of Reaper in apoptotic induction, these findings suggest that Scythe/Reaper may signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules.

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Published In

The EMBO journal

DOI

EISSN

1460-2075

ISSN

0261-4189

Publication Date

March 2001

Volume

20

Issue

5

Start / End Page

1033 / 1041

Related Subject Headings

  • Xenopus Proteins
  • Xenopus
  • Transcription Factors
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Sequence Alignment
  • Recombinant Proteins
  • Recombinant Fusion Proteins
  • Protein Structure, Tertiary
  • Protein Folding
 

Citation

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Thress, K., Song, J., Morimoto, R. I., & Kornbluth, S. (2001). Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper. The EMBO Journal, 20(5), 1033–1041. https://doi.org/10.1093/emboj/20.5.1033
Thress, K., J. Song, R. I. Morimoto, and S. Kornbluth. “Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper.The EMBO Journal 20, no. 5 (March 2001): 1033–41. https://doi.org/10.1093/emboj/20.5.1033.
Thress K, Song J, Morimoto RI, Kornbluth S. Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper. The EMBO journal. 2001 Mar;20(5):1033–41.
Thress, K., et al. “Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper.The EMBO Journal, vol. 20, no. 5, Mar. 2001, pp. 1033–41. Epmc, doi:10.1093/emboj/20.5.1033.
Thress K, Song J, Morimoto RI, Kornbluth S. Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper. The EMBO journal. 2001 Mar;20(5):1033–1041.

Published In

The EMBO journal

DOI

EISSN

1460-2075

ISSN

0261-4189

Publication Date

March 2001

Volume

20

Issue

5

Start / End Page

1033 / 1041

Related Subject Headings

  • Xenopus Proteins
  • Xenopus
  • Transcription Factors
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Sequence Alignment
  • Recombinant Proteins
  • Recombinant Fusion Proteins
  • Protein Structure, Tertiary
  • Protein Folding